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D E Green

Publications and source records attributed to D E Green.

At least 19 recordsLinked to original sources

Ion-channel component of cytochrome oxidase.

Cytochrome oxidase is resolvable into an electron transfer complex and an ion transfer complex. The ion transfer complex has been shown to have the capability for inducing nonspecific ion transport into liposomes. Subunit I of cytochrome oxidase has been identified as an ion-channel-forming protein.

Biological Transport, Active

Patterns of tobacco use in the United States.

Overall, then, the picture of decrease in cigarette smoking is an encouraging one, with the exception of the increased rate of smoking among teenage girls. However, this change probably reflects the tenor of the times and an alteration in the concept of what has traditionally been considered "feminine" behavior.

Adolescent

Resolution of complex III of the mitochondrial electron transfer chain into two component complexes.

Complex III can be resolved into an electron transfer complex and an ion transfer complex. The electron transfer complex contains exclusively the oxidation-reduction proteins of complex III, and the ion transfer complex the capability for augmenting cation-induced fluorescence of 8-anilino-1-naphthalenesulfonic acid. This finding has important implications for the molecular mechanism of mitochondrial energy coupling.

Animals

Resolution of cytochrome oxidase into two component complexes.

Cytochrome c oxidase (ferrocytochrome c: oxygen oxidoreductase, EC 1.9.3.1) has been resolved into a pair of complexes of unequal molecular weight. The larger complex (electron transfer complex) contains exclusively the oxidation-reduction proteins characteristic of cytochrome oxidase; the smaller complex (ion transfer complex) shows exclusively the capability for cation-dependent induction of the fluorescence of 8-anilino-1-naphthalenesulfonic acid--a capability demonstrable in preparations of cytochrome oxidase. The duplex nature of cytochrome oxidase has important implications for the mechanism of energy coupling.

Copper

Uncouplers and the molecular mechanism of uncoupling in mitochondria.

Uncouplers are molecules with protonophoric and ionophoric capabilities that mediate coupled cyclical transport of cations--a transport that takes precedence over all other coupled processes. Uncouplers form cation-containing complexes with electrogenic ionophores that potentiate cyclical transport of cations. The molecular mechanism of uncoupling sheds strong light on the mechanism of coupling.

Adenosine Triphosphatases